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Crystal structure of human TOB1 protein
Analyse Crystal structure of human TOB1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z15
- Type
- protein
- Length
- 476 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein TOB1
- UniProt
- P50616
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein TOB1 | protein | 119 | 42% helix, 18% strand | P50616 |
| B, D | Protein TOB1 | protein | 120 | 47% helix, 20% strand | P50616 |
| C | Protein TOB1 | protein | 117 | 42% helix, 21% strand | P50616 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.72 | 0.92 | 19 | empty |
| 2 | 453 | 0.64 | 0.77 | 49 | empty |
| 3 | 175 | 0.56 | 0.80 | 19 | empty |
| 4 | 172 | 0.51 | 0.78 | 31 | empty |
| 5 | 207 | 0.50 | 0.76 | 28 | empty |
Interfaces
3 interfaces between chains.
- B–C · 799 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 609 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 447 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P50616
- Elsewhere: RCSB PDB 2Z15 · PDBe 2Z15 · UniProt P50616
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